Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/21148
Title: Association of botulinum neurotoxin serotype a light chain with plasma membrane-bound SNAP-25
Authors: Chen, S 
Barbieri, JT
Issue Date: 2011
Publisher: Amer Soc Biochemistry Molecular Biology Inc
Source: Journal of biological chemistry, 2011, v. 286, no. 17, p. 15067-15072 How to cite?
Journal: Journal of Biological Chemistry 
Abstract: The Clostridium botulinum neurotoxins (BoNTs) cleave SNARE proteins, which inhibit binding and thus fusion of neurotransmitter vesicles to the plasma membrane of peripheral neurons. BoNTs comprise an N-terminal light chain (LC) and C-terminal heavy chain, which are linked by a disulfide bond. There are seven serotypes (A-G) of BoNTs based upon immunological neutralization. Although the binding and entry of BoNT/A into neurons has been subjected to considerable investigation, the intracellular events that allow BoNT/A to efficiently cleave SNAP-25 within neurons is less well understood. Earlier studies showed that intracellular LC/A bound to the plasma membrane of neurons. In this study, intracellular LC/A is shown to directly bind SNAP-25 on the plasma membrane. Solid phase binding showed that the N-terminal residues of LC/A bound residues 80-110 of SNAP-25, which was also observed in cultured neurons. Association of the N-terminal 8 amino acids of LC/A and residues 80-110 of SNAP-25 also enhanced substrate cleavage. These findings explain how LC/A associates with SNAP-25 on the plasma membrane and provide a basis for LC/A cleavage of SNAP-25 within the SNARE complex.
URI: http://hdl.handle.net/10397/21148
ISSN: 0021-9258
DOI: 10.1074/jbc.M111.224493
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